Figure 2.
The GPVI collagen-binding interface. (A) Surface representation of the GPVI collagen-binding site (magenta) with residues situated within 4.5 Å of collagen peptide (GPO)5 shown in sticks representation and β-strand labeled in green. (B) Representation of conservation within the GPVI family using ConSurf52 coloring illustrates strict conservation of six central and more variability in five surrounding residues in the collagen-binding site. (C) The GPVI-(GPO)5 interface showing hydrogen bonding interactions and salt bridges (dashed lines) and intermolecular carbon–carbon distances within 4.5 Å (thin solid lines). (GPO)5 residues in the leading (pink), middle (magenta), and trailing (orange) chain are shown in sticks representations and labeled by a sequence number (gray). Also displayed is the (GPO)5 surface, highlighting regions within 4.5 Å of GPVI by coloring according to the nearest chain. GPVI residues in the interface are shown as main chain ribbons and sidechain sticks (blue) and labeled by residue (black). (D-E) Detailed views of the hydrogen bonding interactions between (GPO)5 and GPVI residues Gln71 and Trp76 (D) and Arg38, Glu40, and Arg67 (E). Hydrogen bonds and salt bridges are indicated by dashed lines.

The GPVI collagen-binding interface. (A) Surface representation of the GPVI collagen-binding site (magenta) with residues situated within 4.5 Å of collagen peptide (GPO)5 shown in sticks representation and β-strand labeled in green. (B) Representation of conservation within the GPVI family using ConSurf52 coloring illustrates strict conservation of six central and more variability in five surrounding residues in the collagen-binding site. (C) The GPVI-(GPO)5 interface showing hydrogen bonding interactions and salt bridges (dashed lines) and intermolecular carbon–carbon distances within 4.5 Å (thin solid lines). (GPO)5 residues in the leading (pink), middle (magenta), and trailing (orange) chain are shown in sticks representations and labeled by a sequence number (gray). Also displayed is the (GPO)5 surface, highlighting regions within 4.5 Å of GPVI by coloring according to the nearest chain. GPVI residues in the interface are shown as main chain ribbons and sidechain sticks (blue) and labeled by residue (black). (D-E) Detailed views of the hydrogen bonding interactions between (GPO)5 and GPVI residues Gln71 and Trp76 (D) and Arg38, Glu40, and Arg67 (E). Hydrogen bonds and salt bridges are indicated by dashed lines.

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